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The fourth immunoglobulin-like loop in the extracellular domain of FLT-1, a VEGF receptor, includes a major heparin-binding site.

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Affiliations

  • 1. College of Science, Yonsei University, Seoul, 120-749, Korea.
      Authors
    • Park M 1
    (1 author)

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Biochemical and Biophysical Research Communications, 01 Nov 1999, 264(3):730-734
https://doi.org/10.1006/bbrc.1999.1580 PMID: 10544000 

Abstract 

We found that heparin at low concentrations increases the vascular endothelial growth factor (VEGF)-induced proliferation of human umbilical vein endothelial cells (HUVECs) but at high concentrations decreases it. To examine whether FLT-1, a VEGF receptor, interacts with heparin and which domain of FLT-1 binds to heparin, various extracellular domains of FLT-1 were expressed in a baculovirus/insect cell system: sFLT-1(1-7), sFLT-1(1-4), sFLT-1(1-3), and sFLT-1(1-2) containing immunoglobulin (Ig)-like loop one to seven, one to four, one to three, and one to two, respectively. The sFLT-1(1-7) and sFLT-1(1-4) readily bound heparin at the physiological salt concentration and half-dissociated from heparin at 0.65 M and 0.57 M NaCl, respectively. In contrast, the sFLT-1(1-3) and sFLT-1(1-2) poorly bound heparin at the physiological salt concentration. In addition, the interaction of sFLT-1(1-7) with heparin was not affected by EDTA up to 80 mM. We thus concluded that the fourth Ig-like loop of FLT-1 is a major heparin-binding site and divalent cations are not involved in the interaction of FLT-1 and heparin.

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Read article at publisher's site: https://doi.org/10.1006/bbrc.1999.1580

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